Human cyclophilin 40 unravels neurotoxic amyloids
نویسندگان
چکیده
منابع مشابه
Human cyclophilin 40 unravels neurotoxic amyloids
The accumulation of amyloidogenic proteins is a pathological hallmark of neurodegenerative disorders. The aberrant accumulation of the microtubule associating protein tau (MAPT, tau) into toxic oligomers and amyloid deposits is a primary pathology in tauopathies, the most common of which is Alzheimer's disease (AD). Intrinsically disordered proteins, like tau, are enriched with proline residues...
متن کاملCyclophilin 40 facilitates HSP90-mediated RISC assembly in plants.
Posttranscriptional gene silencing is mediated by RNA-induced silencing complexes (RISCs) that contain AGO proteins and single-stranded small RNAs. The assembly of plant AGO1-containing RISCs depends on the molecular chaperone HSP90. Here, we demonstrate that cyclophilin 40 (CYP40), protein phosphatase 5 (PP5), and several other proteins with the tetratricopeptide repeat (TPR) domain associates...
متن کاملCyclophilin 40 is required for microRNA activity in Arabidopsis.
Loss-of-function mutations of SQUINT (SQN)-which encodes the Arabidopsis orthologue of cyclophilin 40 (CyP40)-cause the precocious expression of adult vegetative traits, an increase in carpel number, and produce abnormal spacing of flowers in the inflorescence. Here we show that the vegetative phenotype of sqn is attributable to the elevated expression of miR156-regulated members of the SPL fam...
متن کاملUbiquitous Amyloids
The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease. On the other hand, organisms take advantage of the strength and dura...
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The term amyloidosis is used to refer to a family of pathologies altering the homeostasis of human organs. Despite having a name that alludes to starch content, the amyloid accumulations are made up of proteins that polymerize as long and rigid fibers. Amyloid proteins vary widely with respect to their amino acid sequences but they share similarities in their quaternary structure; the amyloid f...
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ژورنال
عنوان ژورنال: PLOS Biology
سال: 2017
ISSN: 1545-7885
DOI: 10.1371/journal.pbio.2001336